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Gene Review

DCN  -  decorin

Sus scrofa

 
 
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High impact information on DCN

  • It is concluded that the membrane conductances of DCN pyramidal cells are capable of generating at least 3 discharge patterns (regular firing, long first spike latency, and long first interspike interval) depending on the state of the membrane potential prior to a depolarizing current step [1].
  • The high-affinity uptake and electrically evoked release of exogenous [14C]glycine were measured in vitro in the three major subdivisions of the guinea pig CN: the anteroventral, posteroventral, and dorsal cochlear nuclei (AVCN, PVCN, and DCN, respectively) [2].
  • Anulus fibrosus cells responded to mechanical deformation at the 30-h time point, with increasing gene expression for types I and II collagen, aggrecan, biglycan, decorin and lumican [3].
  • Prevention of IGF-1 and TGFbeta stimulated type II collagen and decorin expression by bFGF and identification of IGF-1 mRNA transcripts in articular chondrocytes [4].
  • OBJECTIVES: the aim of this investigation was to establish whether the action of bFGF modulated the production of type II collagen, decorin and biglycan induced by IGF-1 or TGFbeta in porcine articular chondrocytes [4].
 

Biological context of DCN

  • Changes in the expression of the transcription factors preceded the induction of integrin alpha2 and the down-regulation of decorin, while mRNAs for laminin beta1 and osteopontin rose immediately after serum stimulation [5].
  • The small leucine-rich proteoglycan, decorin, was identified as one of the proteoglycans, in addition to others of higher molecular weight, by cross-reaction with an antiserum raised against pig laryngeal decorin and by N-terminal amino acid sequencing [6].
 

Anatomical context of DCN

  • These residual activities in the DCN may be mediated by the axonal endings of the granule cells of the cochlear nucleus [7].
  • The specific binding of [(3)H]strychnine was measured in slices of the dorsal (DCN), posteroventral (PVCN) and anteroventral (AVCN) cochlear nucleus (CN), the lateral (LSO) and medial (MSO) superior olive, and the inferior colliculus (IC) 145 days after UCA [8].
  • Proteoglycans such as versican, decorin, and perlecan are important components of the extracellular matrix in various tissues [9].
 

Associations of DCN with chemical compounds

  • Substitution of chondroitin-6-sulfate by either dermatan sulfate or decorin increased the delay in wound contraction by the greatest increment [10].
  • Biglycan and decorin, two related dermatan sulphate proteoglycans, were identified in the small proteoglycan pool by their behaviour on gel electrophoresis and by immunostaining with specific antibodies [11].
  • The PG eluting earliest from Octyl-Sepharose was identified as decorin on the basis of the size of the protein core produced by digestion with chondroitinase ABC, its recognition by monoclonal antibodies raised against bovine decorin and its N-terminal sequence, 23 of 24 amino acids of which were identified [12].
  • This GAG is commonly found in the collagen-associated proteoglycan decorin, which is likely well crosslinked by glutaraldehyde [13].
  • Decorin was isolated from 7 M urea extract of bovine placental cotyledons by ion-exchange and hydrophobic chromatography [14].
 

Other interactions of DCN

  • Expression of aggrecan, COMP, decorin, and Col10a1 increased significantly within 52 weeks [15].
  • Genes for the small proteoglycans, biglycan, and decorin, but not lumican, were up-regulated in transition zone cells following incubation in either hypo- or hyper-osmotic media [16].
 

Analytical, diagnostic and therapeutic context of DCN

  • Anti-decorin core protein antiserum from pig skin was reacted with placental decorin and its core protein in western blotting [14].
  • Decorin and its core protein showed a broad band at about 115 kDa and a single band at 47 kDa, respectively by SDS-PAGE [14].

References

  1. Membrane properties and discharge characteristics of guinea pig dorsal cochlear nucleus neurons studied in vitro. Manis, P.B. J. Neurosci. (1990) [Pubmed]
  2. Uptake and release of glycine in the guinea pig cochlear nucleus after axotomy of afferent or centrifugal fibers. Staatz-Benson, C., Potashner, S.J. J. Neurochem. (1988) [Pubmed]
  3. Static compression induces zonal-specific changes in gene expression for extracellular matrix and cytoskeletal proteins in intervertebral disc cells in vitro. Chen, J., Yan, W., Setton, L.A. Matrix Biol. (2004) [Pubmed]
  4. Prevention of IGF-1 and TGFbeta stimulated type II collagen and decorin expression by bFGF and identification of IGF-1 mRNA transcripts in articular chondrocytes. Sonal, D. Matrix Biol. (2001) [Pubmed]
  5. Expression of transcription factors and matrix genes in response to serum stimulus in vascular smooth muscle cells. Markmann, A., Rauterberg, J., Vischer, P., Robenek, H., Echtermeyer, F., Will, H., Seidler, D.G., Young, M.F., Kresse, H. Eur. J. Cell Biol. (2003) [Pubmed]
  6. Decorin is one of the proteoglycans expressed in Walker 256 rat mammary carcinoma. Oba-Shinjo, S.M., Berto, A.G., Passerotti, C.C., Barbosa, C.D., Sampaio, L.O. Braz. J. Med. Biol. Res. (2003) [Pubmed]
  7. Uptake and release of D-aspartate in the guinea pig cochlear nucleus. Potashner, S.J. J. Neurochem. (1983) [Pubmed]
  8. Protein kinases regulate glycine receptor binding in brain stem auditory nuclei after unilateral cochlear ablation. Yan, L., Suneja, S.K., Potashner, S.J. Brain Res. (2007) [Pubmed]
  9. Ultrastructure of proteoglycans in tissue-engineered cardiovascular structures. Rothenburger, M., Völker, W., Vischer, P., Glasmacher, B., Scheld, H.H., Deiwick, M. Tissue engineering. (2002) [Pubmed]
  10. Specific effects of glycosaminoglycans in an analog of extracellular matrix that delays wound contraction and induces regeneration. Shafritz, T.A., Rosenberg, L.C., Yannas, I.V. Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society (1994) [Pubmed]
  11. Glycosaminoglycans and proteoglycans from different zones of the porcine knee meniscus. Nakano, T., Dodd, C.M., Scott, P.G. J. Orthop. Res. (1997) [Pubmed]
  12. Isolation and characterization of small proteoglycans from different zones of the porcine knee meniscus. Scott, P.G., Nakano, T., Dodd, C.M. Biochim. Biophys. Acta (1997) [Pubmed]
  13. Loss of chondroitin 6-sulfate and hyaluronan from failed porcine bioprosthetic valves. Grande-Allen, K.J., Mako, W.J., Calabro, A., Shi, Y., Ratliff, N.B., Vesely, I. Journal of biomedical materials research. Part A. (2003) [Pubmed]
  14. Affinity of placental decorin for collagen. Batbayar, T., Nomura, Y., Ishii, Y., Shirai, K. Biosci. Biotechnol. Biochem. (2000) [Pubmed]
  15. Molecular characterization of spontaneous and growth-factor-augmented chondrogenesis in periosteum-bone tissue transferred into a joint. Jung, M., Gotterbarm, T., Gruettgen, A., Vilei, S.B., Breusch, S., Richter, W. Histochem. Cell Biol. (2005) [Pubmed]
  16. Matrix protein gene expression in intervertebral disc cells subjected to altered osmolarity. Chen, J., Baer, A.E., Paik, P.Y., Yan, W., Setton, L.A. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
 
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